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PMID: 2822721 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Mechanism of activation of lymphocyte Na+/H+ exchange by concanavalin A. A calcium- and protein kinase C-independent pathway.

The Journal of biological chemistry ·Vol. 262 ·No. 31 ·1987-11-05 ·Pages 15277-84

Grinstein S, Smith JD, Rowatt C, Dixon SJ

Abstract

Treatment of thymic lymphocytes with the mitogenic lectin concanavalin A (ConA) increases the intracellular free Ca2+ concentration and stimulates phosphoinositide turnover. ConA also induced a rapid, amiloride-sensitive, Na+-dependent increase in cytosolic pH of 0.13 +/- 0.01, indicative of stimulation of the Na+/H+ antiport. To investigate the mechanism underlying activation of Na+/H+ exchange by ConA, the intracellular free Ca2+ concentration changes induced by this lectin were precluded by loading the cells with Ca2+-buffering agents and suspension in Ca2+-free media. Under these conditions, the ConA-induced cytoplasmic alkalinization proceeded normally. Two approaches were used to assess the role of protein kinase C. First, this enzyme was inhibited by the addition of 1-(5-isoquinolinysulfonyl)-2-methylpiperazine. In the presence of this potent antagonist, stimulation of the antiport by 12-O-tetradecanoylphorbol-13-acetate was greatly inhibited. In contrast, stimulation by ConA was unaffected. Second, protein kinase C was depleted by overnight incubation with phorbol esters. Following this treatment, Na+/H+ exchange was no longer activated by 12-O-tetradecanoyl-13-acetate, but was still stimulated by ConA. These data suggest that a Ca2+- and protein kinase C-independent mechanisms mediates the activation of Na+/H+ exchange by ConA. The possible role of GTP-binding proteins in the activation was also studied. The antiport was not stimulated by either fluoroaluminate or vanadate. Moreover, pretreatment with pertussis toxin failed to inhibit the ConA-induced cytoplasmic alkalinization. In contrast, preincubation with cholera toxin partially inhibited activation. Under these conditions, cholera toxin significantly elevated intracellular cAMP levels. Inhibition was also observed in cells treated with forskolin at concentrations that increased [cAMP]. The data suggest that a novel cAMP-sensitive signaling mechanism not involving Ca2+ and protein kinase C is involved in the stimulation of Na+/H+ exchange by mitogens in T lymphocytes.

MeSH Terms
Animals Calcium/metabolism Carrier Proteins/metabolism Cells, Cultured Cholera Toxin/pharmacology Colforsin/pharmacology Concanavalin A/pharmacology Cyclic AMP/physiology Cytoplasm/metabolism Ethers/pharmacology Hydrogen-Ion Concentration Ionomycin Kinetics Male Pertussis Toxin Protein Kinase C/metabolism Rats Sodium-Hydrogen Exchangers T-Lymphocytes/drug effects,immunology,metabolism Virulence Factors, Bordetella/pharmacology
Chemicals
Carrier Proteins Ethers Sodium-Hydrogen Exchangers Virulence Factors, Bordetella Concanavalin A Colforsin Ionomycin Cholera Toxin Cyclic AMP Pertussis Toxin Protein Kinase C Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Grinstein S
Department of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada.
Smith J D
Rowatt C
Dixon S J
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1987-11-05
Pages
15277-84
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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